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P16050

- LOX15_HUMAN

UniProt

P16050 - LOX15_HUMAN

Protein

Arachidonate 15-lipoxygenase

Gene

ALOX15

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Converts arachidonic acid into 12-hydroperoxyeicosatetraenoic acid/12-HPETE and 15-hydroperoxyeicosatetraenoic acid/15-HPETE. Also converts linoleic acid to 13-hydroperoxyoctadecadienoic acid. May also act on (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE to produce hepoxilin A3. Probably plays an important role in the immune and inflammatory responses. Through the oxygenation of membrane-bound phosphatidylethanolamine in macrophages may favor clearance of apoptotic cells during inflammation by resident macrophages and prevent an autoimmune response associated with the clearance of apoptotic cells by inflammatory monocytes. In parallel, may regulate actin polymerization which is crucial for several biological processes, including macrophage function. May also regulate macrophage function through regulation of the peroxisome proliferator activated receptor signaling pathway. Finally, it is also involved in the cellular response to IL13/interleukin-13. In addition to its role in the immune and inflammatory responses, may play a role in epithelial wound healing in the cornea maybe through production of lipoxin A4. May also play a role in endoplasmic reticulum stress response and the regulation of bone mass.2 Publications

    Catalytic activityi

    Arachidonate + O2 = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate.
    Arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate.

    Cofactori

    Binds 1 iron ion per subunit.PROSITE-ProRule annotation

    Enzyme regulationi

    Activity is increased by binding phosphatidylinositol phosphates, especially phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi360 – 3601Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi365 – 3651Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi540 – 5401Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi544 – 5441Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi662 – 6621Iron; via carboxylate; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. arachidonate 12-lipoxygenase activity Source: UniProtKB
    2. arachidonate 15-lipoxygenase activity Source: UniProtKB
    3. eoxin A4 synthase activity Source: Reactome
    4. iron ion binding Source: UniProtKB
    5. phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
    6. protein binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic cell clearance Source: UniProtKB
    2. arachidonic acid metabolic process Source: UniProtKB
    3. bone mineralization Source: UniProtKB
    4. cellular response to calcium ion Source: UniProtKB
    5. cellular response to interleukin-13 Source: UniProtKB
    6. hepoxilin biosynthetic process Source: UniProtKB
    7. inflammatory response Source: ProtInc
    8. leukotriene metabolic process Source: Reactome
    9. lipoxin A4 biosynthetic process Source: UniProtKB
    10. lipoxygenase pathway Source: UniProtKB
    11. negative regulation of adaptive immune response Source: UniProtKB
    12. ossification Source: UniProtKB
    13. phosphatidylethanolamine biosynthetic process Source: UniProtKB
    14. positive regulation of actin filament polymerization Source: UniProtKB
    15. positive regulation of cell-substrate adhesion Source: UniProtKB
    16. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    17. regulation of engulfment of apoptotic cell Source: UniProtKB
    18. regulation of peroxisome proliferator activated receptor signaling pathway Source: UniProtKB
    19. response to endoplasmic reticulum stress Source: UniProtKB
    20. small molecule metabolic process Source: Reactome
    21. wound healing Source: UniProtKB

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    Calcium, Iron, Lipid-binding, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08621-MONOMER.
    ReactomeiREACT_150201. Synthesis of 12-eicosatetraenoic acid derivatives.
    REACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
    REACT_150422. Synthesis of 15-eicosatetraenoic acid derivatives.
    UniPathwayiUPA00881.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arachidonate 15-lipoxygenase (EC:1.13.11.33)
    Short name:
    15-LOX
    Short name:
    15-LOX-1
    Alternative name(s):
    12/15-lipoxygenase
    Arachidonate 12-lipoxygenase, leukocyte-type (EC:1.13.11.31)
    Short name:
    12-LOX
    Arachidonate omega-6 lipoxygenase
    Gene namesi
    Name:ALOX15
    Synonyms:LOG15
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:433. ALOX15.

    Subcellular locationi

    Cytoplasmcytosol. Cell membrane; Peripheral membrane protein. Lipid droplet
    Note: Predominantly cytosolic; becomes enriched at membranes upon calcium binding. Translocates from the cytosol to the plasma membrane when stimulated by IL13/interleukin-13 and in macrophages binding apoptotic cells.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
    3. lipid particle Source: UniProtKB
    4. membrane Source: UniProtKB
    5. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Lipid droplet, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Disease susceptibility may be associated with variations affecting the gene represented in this entry. Met at position 560 may confer interindividual susceptibility to coronary artery disease (CAD) (PubMed:17959182).1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi418 – 4181M → V: Catalyzes 15- and 12-lipoxygenation. 1 Publication

    Organism-specific databases

    PharmGKBiPA48.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 662661Arachidonate 15-lipoxygenasePRO_0000220697Add
    BLAST

    Proteomic databases

    PaxDbiP16050.
    PRIDEiP16050.

    PTM databases

    PhosphoSiteiP16050.

    Expressioni

    Tissue specificityi

    Detected in monocytes and eosinophils (at protein level). Expressed in airway epithelial cells.2 Publications

    Inductioni

    Up-regulated by UV-irradiation.1 Publication

    Gene expression databases

    ArrayExpressiP16050.
    BgeeiP16050.
    CleanExiHS_ALOX15.
    GenevestigatoriP16050.

    Organism-specific databases

    HPAiCAB004962.
    CAB004963.
    HPA013859.

    Interactioni

    Subunit structurei

    Interacts with PEBP1; in response to IL13/interleukin-13, prevents the interaction of PEBP1 with RAF1 to activate the ERK signaling cascade.1 Publication

    Protein-protein interaction databases

    DIPiDIP-60388N.
    STRINGi9606.ENSP00000293761.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ABTmodel-A2-662[»]
    ProteinModelPortaliP16050.
    SMRiP16050. Positions 2-662.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 114113PLATPROSITE-ProRule annotationAdd
    BLAST
    Domaini115 – 662548LipoxygenasePROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The PLAT domain can bind calcium ions; this promotes association with membranes.By similarity

    Sequence similaritiesi

    Belongs to the lipoxygenase family.Curated
    Contains 1 lipoxygenase domain.PROSITE-ProRule annotation
    Contains 1 PLAT domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG133298.
    HOVERGENiHBG005150.
    InParanoidiP16050.
    KOiK00460.
    OrthoDBiEOG7B05CG.
    PhylomeDBiP16050.
    TreeFamiTF105320.

    Family and domain databases

    Gene3Di2.60.60.20. 1 hit.
    InterProiIPR008976. Lipase_LipOase.
    IPR000907. LipOase.
    IPR013819. LipOase_C.
    IPR020834. LipOase_CS.
    IPR020833. LipOase_Fe_BS.
    IPR001885. LipOase_mml.
    IPR001024. PLAT/LH2_dom.
    [Graphical view]
    PANTHERiPTHR11771. PTHR11771. 1 hit.
    PfamiPF00305. Lipoxygenase. 2 hits.
    PF01477. PLAT. 1 hit.
    [Graphical view]
    PRINTSiPR00087. LIPOXYGENASE.
    PR00467. MAMLPOXGNASE.
    SMARTiSM00308. LH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF48484. SSF48484. 1 hit.
    SSF49723. SSF49723. 1 hit.
    PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
    PS00081. LIPOXYGENASE_2. 1 hit.
    PS51393. LIPOXYGENASE_3. 1 hit.
    PS50095. PLAT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P16050-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGLYRIRVST GASLYAGSNN QVQLWLVGQH GEAALGKRLW PARGKETELK    50
    VEVPEYLGPL LFVKLRKRHL LKDDAWFCNW ISVQGPGAGD EVRFPCYRWV 100
    EGNGVLSLPE GTGRTVGEDP QGLFQKHREE ELEERRKLYR WGNWKDGLIL 150
    NMAGAKLYDL PVDERFLEDK RVDFEVSLAK GLADLAIKDS LNVLTCWKDL 200
    DDFNRIFWCG QSKLAERVRD SWKEDALFGY QFLNGANPVV LRRSAHLPAR 250
    LVFPPGMEEL QAQLEKELEG GTLFEADFSL LDGIKANVIL CSQQHLAAPL 300
    VMLKLQPDGK LLPMVIQLQL PRTGSPPPPL FLPTDPPMAW LLAKCWVRSS 350
    DFQLHELQSH LLRGHLMAEV IVVATMRCLP SIHPIFKLII PHLRYTLEIN 400
    VRARTGLVSD MGIFDQIMST GGGGHVQLLK QAGAFLTYSS FCPPDDLADR 450
    GLLGVKSSFY AQDALRLWEI IYRYVEGIVS LHYKTDVAVK DDPELQTWCR 500
    EITEIGLQGA QDRGFPVSLQ ARDQVCHFVT MCIFTCTGQH ASVHLGQLDW 550
    YSWVPNAPCT MRLPPPTTKD ATLETVMATL PNFHQASLQM SITWQLGRRQ 600
    PVMVAVGQHE EEYFSGPEPK AVLKKFREEL AALDKEIEIR NAKLDMPYEY 650
    LRPSVVENSV AI 662
    Length:662
    Mass (Da):74,804
    Last modified:January 23, 2007 - v3
    Checksum:i9ACF7FE7863A045C
    GO
    Isoform 2 (identifier: P16050-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         46-84: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:623
    Mass (Da):70,108
    Checksum:i71B99C6D8E707189
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti46 – 461E → V in AAC52118. (PubMed:9700053)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti90 – 901D → H.1 Publication
    Corresponds to variant rs11568142 [ dbSNP | Ensembl ].
    VAR_018746
    Natural varianti102 – 1021G → V.
    Corresponds to variant rs41439950 [ dbSNP | Ensembl ].
    VAR_035036
    Natural varianti103 – 1031N → K.1 Publication
    Corresponds to variant rs11568099 [ dbSNP | Ensembl ].
    VAR_018747
    Natural varianti205 – 2051R → Q.1 Publication
    Corresponds to variant rs11568101 [ dbSNP | Ensembl ].
    VAR_018748
    Natural varianti239 – 2391V → M.
    Corresponds to variant rs3892408 [ dbSNP | Ensembl ].
    VAR_035037
    Natural varianti461 – 4611A → P.1 Publication
    Corresponds to variant rs17852628 [ dbSNP | Ensembl ].
    VAR_035038
    Natural varianti560 – 5601T → M Loss of catalytic activity. 1 Publication
    Corresponds to variant rs34210653 [ dbSNP | Ensembl ].
    VAR_035039

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei46 – 8439Missing in isoform 2. 1 PublicationVSP_056681Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M23892 mRNA. Translation: AAA36182.1.
    U88317 Genomic DNA. Translation: AAB49305.1.
    AK290309 mRNA. Translation: BAF82998.1.
    AK316126 mRNA. Translation: BAH14497.1.
    AY505111 Genomic DNA. Translation: AAR84235.1.
    AC118754 Genomic DNA. No translation available.
    BC029032 mRNA. Translation: AAH29032.1.
    U63384 Genomic DNA. Translation: AAC52118.1.
    CCDSiCCDS11049.1.
    PIRiA31349.
    RefSeqiNP_001131.3. NM_001140.3.
    UniGeneiHs.73809.

    Genome annotation databases

    EnsembliENST00000293761; ENSP00000293761; ENSG00000161905.
    ENST00000570836; ENSP00000458832; ENSG00000161905.
    ENST00000574640; ENSP00000460483; ENSG00000161905.
    GeneIDi246.
    KEGGihsa:246.
    UCSCiuc002fyh.3. human.

    Polymorphism databases

    DMDMi126396.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M23892 mRNA. Translation: AAA36182.1 .
    U88317 Genomic DNA. Translation: AAB49305.1 .
    AK290309 mRNA. Translation: BAF82998.1 .
    AK316126 mRNA. Translation: BAH14497.1 .
    AY505111 Genomic DNA. Translation: AAR84235.1 .
    AC118754 Genomic DNA. No translation available.
    BC029032 mRNA. Translation: AAH29032.1 .
    U63384 Genomic DNA. Translation: AAC52118.1 .
    CCDSi CCDS11049.1.
    PIRi A31349.
    RefSeqi NP_001131.3. NM_001140.3.
    UniGenei Hs.73809.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ABT model - A 2-662 [» ]
    ProteinModelPortali P16050.
    SMRi P16050. Positions 2-662.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60388N.
    STRINGi 9606.ENSP00000293761.

    Chemistry

    BindingDBi P16050.
    ChEMBLi CHEMBL2903.
    DrugBanki DB01188. Ciclopirox.
    DB00179. Masoprocol.
    DB00744. Zileuton.

    PTM databases

    PhosphoSitei P16050.

    Polymorphism databases

    DMDMi 126396.

    Proteomic databases

    PaxDbi P16050.
    PRIDEi P16050.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000293761 ; ENSP00000293761 ; ENSG00000161905 .
    ENST00000570836 ; ENSP00000458832 ; ENSG00000161905 .
    ENST00000574640 ; ENSP00000460483 ; ENSG00000161905 .
    GeneIDi 246.
    KEGGi hsa:246.
    UCSCi uc002fyh.3. human.

    Organism-specific databases

    CTDi 246.
    GeneCardsi GC17M004534.
    HGNCi HGNC:433. ALOX15.
    HPAi CAB004962.
    CAB004963.
    HPA013859.
    MIMi 152392. gene.
    neXtProti NX_P16050.
    PharmGKBi PA48.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG133298.
    HOVERGENi HBG005150.
    InParanoidi P16050.
    KOi K00460.
    OrthoDBi EOG7B05CG.
    PhylomeDBi P16050.
    TreeFami TF105320.

    Enzyme and pathway databases

    UniPathwayi UPA00881 .
    BioCyci MetaCyc:HS08621-MONOMER.
    Reactomei REACT_150201. Synthesis of 12-eicosatetraenoic acid derivatives.
    REACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
    REACT_150422. Synthesis of 15-eicosatetraenoic acid derivatives.

    Miscellaneous databases

    GeneWikii ALOX15.
    GenomeRNAii 246.
    NextBioi 979.
    PROi P16050.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16050.
    Bgeei P16050.
    CleanExi HS_ALOX15.
    Genevestigatori P16050.

    Family and domain databases

    Gene3Di 2.60.60.20. 1 hit.
    InterProi IPR008976. Lipase_LipOase.
    IPR000907. LipOase.
    IPR013819. LipOase_C.
    IPR020834. LipOase_CS.
    IPR020833. LipOase_Fe_BS.
    IPR001885. LipOase_mml.
    IPR001024. PLAT/LH2_dom.
    [Graphical view ]
    PANTHERi PTHR11771. PTHR11771. 1 hit.
    Pfami PF00305. Lipoxygenase. 2 hits.
    PF01477. PLAT. 1 hit.
    [Graphical view ]
    PRINTSi PR00087. LIPOXYGENASE.
    PR00467. MAMLPOXGNASE.
    SMARTi SM00308. LH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48484. SSF48484. 1 hit.
    SSF49723. SSF49723. 1 hit.
    PROSITEi PS00711. LIPOXYGENASE_1. 1 hit.
    PS00081. LIPOXYGENASE_2. 1 hit.
    PS51393. LIPOXYGENASE_3. 1 hit.
    PS50095. PLAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
    2. "Characterization and sequence of an additional 15-lipoxygenase transcript and of the human gene."
      Kritzik M.R., Ziober A.F., Dicharry S., Conrad D.J., Sigal E.
      Biochim. Biophys. Acta 1352:267-281(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Tongue.
    4. SeattleSNPs variation discovery resource
      Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-90; LYS-103 AND GLN-205.
    5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PRO-461.
      Tissue: Brain and Lung.
    7. "Human 15-lipoxygenase gene promoter: analysis and identification of DNA binding sites for IL-13-induced regulatory factors in monocytes."
      Kelavkar U., Wang S., Montero A., Murtagh J., Shah K., Badr K.
      Mol. Biol. Rep. 25:173-182(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46.
    8. "Arachidonate 15-lipoxygenase (omega-6 lipoxygenase) from human leukocytes. Purification and structural homology to other mammalian lipoxygenases."
      Sigal E., Grunberger D., Craik C.S., Caughey G.H., Nadel J.A.
      J. Biol. Chem. 263:5328-5332(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-16.
    9. "Purification of two forms of arachidonate 15-lipoxygenase from human leukocytes."
      Izumi T., Raadmark O., Joernvall H., Samuelsson B.
      Eur. J. Biochem. 202:1231-1238(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-31; 38-45; 157-168 AND 626-631.
      Tissue: Eosinophil and Leukocyte.
    10. "A primary determinant for lipoxygenase positional specificity."
      Sloane D.L., Leung R., Craik C.S., Sigal E.
      Nature 354:149-152(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF MET-418.
    11. "Membrane translocation of 15-lipoxygenase in hematopoietic cells is calcium-dependent and activates the oxygenase activity of the enzyme."
      Brinckmann R., Schnurr K., Heydeck D., Rosenbach T., Kolde G., Kuehn H.
      Blood 91:64-74(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    12. "Evaluation of the activity and localization of 15-lipoxygenase-1 after introduction into human colorectal carcinoma Caco-2 cells."
      Hsi L.C., Kamitani H., Cornicelli J.A., Eling T.E.
      Prostaglandins Leukot. Essent. Fatty Acids 64:217-225(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    13. "Interaction of human 15-lipoxygenase-1 with phosphatidylinositol bisphosphates results in increased enzyme activity."
      Andersson E., Schain F., Svedling M., Claesson H.E., Forsell P.K.
      Biochim. Biophys. Acta 1761:1498-1505(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: LIPID-BINDING, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION.
    14. "Reciprocal regulation of 12- and 15-lipoxygenases by UV-irradiation in human keratinocytes."
      Yoo H., Jeon B., Jeon M.S., Lee H., Kim T.Y.
      FEBS Lett. 582:3249-3253(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY UV.
    15. "15(S)-Lipoxygenase-1 associates with neutral lipid droplets in macrophage foam cells: evidence of lipid droplet metabolism."
      Weibel G.L., Joshi M.R., Wei C., Bates S.R., Blair I.A., Rothblat G.H.
      J. Lipid Res. 50:2371-2376(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    16. "15-Lipoxygenase 1 interacts with phosphatidylethanolamine-binding protein to regulate MAPK signaling in human airway epithelial cells."
      Zhao J., O'Donnell V.B., Balzar S., St Croix C.M., Trudeau J.B., Wenzel S.E.
      Proc. Natl. Acad. Sci. U.S.A. 108:14246-14251(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN IL13 SIGNALING, INTERACTION WITH PEBP1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    17. Cited for: VARIANT MET-560, CHARACTERIZATION OF VARIANT MET-560, INVOLVEMENT IN CORONARY ARTERY DISEASE.

    Entry informationi

    Entry nameiLOX15_HUMAN
    AccessioniPrimary (citable) accession number: P16050
    Secondary accession number(s): A8K2P4
    , B7ZA11, Q8N6R7, Q99657
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 155 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3